Summary for 7Z8N
| Entry DOI | 10.2210/pdb7z8n/pdb |
| Descriptor | Histidine kinase, CALCIUM ION, R-1,2-PROPANEDIOL, ... (4 entities in total) |
| Functional Keywords | histidine kinase hamp domain coiled-coil gacs pseudomonas aeruginosa, signaling protein |
| Biological source | Pseudomonas aeruginosa PAO1 |
| Total number of polymer chains | 4 |
| Total formula weight | 141906.05 |
| Authors | Fadel, F.,Bassim, V.,Francis, V.I.,Porter, S.L.,Botzanowski, T.,Legrand, P.,Bourne, Y.,Cianferani, S.,Vincent, F. (deposition date: 2022-03-17, release date: 2022-07-13, Last modification date: 2023-01-25) |
| Primary citation | Fadel, F.,Bassim, V.,Francis, V.I.,Porter, S.L.,Botzanowski, T.,Legrand, P.,Perez, M.M.,Bourne, Y.,Cianferani, S.,Vincent, F. Insights into the atypical autokinase activity of the Pseudomonas aeruginosa GacS histidine kinase and its interaction with RetS. Structure, 30:1285-1297.e5, 2022 Cited by PubMed Abstract: Virulence in Pseudomonas aeruginosa (PA) depends on complex regulatory networks, involving phosphorelay systems based on two-component systems (TCSs). The GacS/GacA TCS is a master regulator of biofilm formation, swarming motility, and virulence. GacS is a membrane-associated unorthodox histidine kinase (HK) whose phosphorelay signaling pathway is inhibited by the RetS hybrid HK. Here we provide structural and functional insights into the interaction of GacS with RetS. The structure of the GacS-HAMP-H1 cytoplasmic regions reveals an unusually elongated homodimer marked by a 135 Å long helical bundle formed by the HAMP, the signaling helix (S helix) and the DHp subdomain. The HAMP and S helix regions are essential for GacS signaling and contribute to the GacS/RetS binding interface. The structure of the GacS D1 domain together with the discovery of an unidentified functional ND domain, essential for GacS full autokinase activity, unveils signature motifs in GacS required for its atypical autokinase mechanism. PubMed: 35767996DOI: 10.1016/j.str.2022.06.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.64 Å) |
Structure validation
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